Crystal structure of EGFR kinase domain in complex with compound 3g
The structure was published by Peng, Y.H., Shiao, H.Y., Tu, C.H., et al., Lyu, P.C., Hsieh, H.P., and Wu, S.Y., in 2013 in a paper entitled "Protein Kinase Inhibitor Design by Targeting the Asp-Phe-Gly (DFG) Motif: The Role of the DFG Motif in the Design of Epidermal Growth Factor Receptor Inhibitors" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2013.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Epidermal growth factor receptor. This molecule has the UniProt identifier P00533 (EGFR_HUMAN). The sample contained 328 residues which is < 90% of the natural sequence. Out of 328 residues 303 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: